Research Article

Interplaying factors for the formation of photoswitchable β-hairpins: the advantage of a flexible switch

  1. Miranda Varedian1,
  2. Máté Erdélyi1,2,
  3. Åsa Persson2,
  4. Adolf Gogoll1,*

Article first published online: 17 DEC 2008

DOI: 10.1002/psc.1103

Issue

Journal of Peptide Science

Journal of Peptide Science

Volume 15, Issue 2, pages 107–113, February 2009

Additional Information

How to Cite

Varedian, M., Erdélyi, M., Persson, Å. and Gogoll, A. (2009), Interplaying factors for the formation of photoswitchable β-hairpins: the advantage of a flexible switch. Journal of Peptide Science, 15: 107–113. doi: 10.1002/psc.1103

Author Information

  1. 1

    Department of Biochemistry and Organic Chemistry, Uppsala University, Box 576, 751 23 Uppsala, Sweden

  2. 2

    Department of Medicinal Chemistry, Uppsala University, Box 574, 751 23 Uppsala, Sweden

*Department of Biochemistry and Organic Chemistry, Uppsala University, Box 576, 751 23 Uppsala, Sweden.

Publication History

  1. Issue published online: 9 JAN 2009
  2. Article first published online: 17 DEC 2008
  3. Manuscript Accepted: 4 NOV 2008
  4. Manuscript Revised: 6 OCT 2008
  5. Manuscript Received: 18 AUG 2008

Funded by

  • Swedish Research Council. Grant Number: 621-2006-3877

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Keywords:

  • peptidomimetics;
  • conformational analysis;
  • photoswitches;
  • diffusion coefficients;
  • CD

Abstract

A series of peptidomimetics intended to promote the β-hairpin motif have been studied. Structural variations include a turn region with and without a photoswitchable chromophore, and strands with amino acid side chains supporting various degrees of interstrand interactions for hairpin stabilisation. The propensity of the compounds to form β-hairpins was evaluated experimentally by NMR spectroscopy, translational self-diffusion studies and CD spectroscopy. In the presence of hairpin stabilising interstrand interactions, the structurally flexible stilbene chromophore appeared to be well compatible with the imposed secondary structure. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.

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